PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23634831-3	2013	Previously we showed that trypanosomatid S-adenosylmethionine decarboxylase (AdoMetDC), a key enzyme for biosynthesis of the polyamine spermidine, is activated by heterodimer formation with an inactive paralogue termed prozyme.	polyamine spermidine	125-145	adenosylmethionine decarboxylase 1	Homo sapiens	77-85	
23288847-4	2013	S-adenosylmethionine decarboxylase (AdoMetDC) catalyzes a key step in the production of the polyamine spermidine.	polyamine spermidine	92-112	adenosylmethionine decarboxylase 1	Homo sapiens	0-34	
23288847-4	2013	S-adenosylmethionine decarboxylase (AdoMetDC) catalyzes a key step in the production of the polyamine spermidine.	polyamine spermidine	92-112	adenosylmethionine decarboxylase 1	Homo sapiens	36-44